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K Breddam

Showing results (1-10 of 52) with videos related to

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Carlsberg Research Communications|January 1, 1988
Carboxypeptidase S-1 from Penicillium janthinellum: enzymatic properties in hydrolysis and aminolysis reactionsK Breddam
European Journal of Biochemistry|May 15, 1992
Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenchingK Breddam, M Meldal
Biochemistry|October 7, 1997
Substrates with charged P1 residues are efficiently hydrolyzed by serine carboxypeptidases when S3-P1 interactions are facilitatedK Olesen, K Breddam
European Journal of Biochemistry|February 15, 1992
Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformisI Svendsen, K Breddam
Analytical Biochemistry|September 15, 1998
Peptide substrates dissolved in dimethylformamide may be modified at the epsilon-amino group of lysyl residues, causing erroneous kinetic characterization of proteolytic enzymesK Olesen, K Breddam
Biochemistry|December 5, 1995
Increase of the P1 Lys/Leu substrate preference of carboxypeptidase Y by rational design based on known primary and tertiary structures of serine carboxypeptidasesK Olesen, K Breddam
Biochemistry|September 22, 1992
Interdependency of the binding subsites in subtilisinH Grøn, K Breddam
Analytical Biochemistry|May 15, 1991
Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsinM Meldal, K Breddam
Protein Science : a Publication of the Protein Society|May 1, 1994
A conserved glutamic acid bridge in serine carboxypeptidases, belonging to the alpha/beta hydrolase fold, acts as a pH-dependent protein-stabilizing elementU H Mortensen, K Breddam
Methods in Enzymology|January 1, 1994
Glutamyl endopeptidasesJ J Birktoft, K Breddam
Pageof 6

Showing results (1-10 of 52) with videos related to

Sort By:
Pageof 6
Carlsberg Research Communications|January 1, 1988
Carboxypeptidase S-1 from Penicillium janthinellum: enzymatic properties in hydrolysis and aminolysis reactionsK Breddam
European Journal of Biochemistry|May 15, 1992
Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenchingK Breddam, M Meldal
Biochemistry|October 7, 1997
Substrates with charged P1 residues are efficiently hydrolyzed by serine carboxypeptidases when S3-P1 interactions are facilitatedK Olesen, K Breddam
European Journal of Biochemistry|February 15, 1992
Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformisI Svendsen, K Breddam
Analytical Biochemistry|September 15, 1998
Peptide substrates dissolved in dimethylformamide may be modified at the epsilon-amino group of lysyl residues, causing erroneous kinetic characterization of proteolytic enzymesK Olesen, K Breddam
Biochemistry|December 5, 1995
Increase of the P1 Lys/Leu substrate preference of carboxypeptidase Y by rational design based on known primary and tertiary structures of serine carboxypeptidasesK Olesen, K Breddam
Biochemistry|September 22, 1992
Interdependency of the binding subsites in subtilisinH Grøn, K Breddam
Analytical Biochemistry|May 15, 1991
Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsinM Meldal, K Breddam
Protein Science : a Publication of the Protein Society|May 1, 1994
A conserved glutamic acid bridge in serine carboxypeptidases, belonging to the alpha/beta hydrolase fold, acts as a pH-dependent protein-stabilizing elementU H Mortensen, K Breddam
Methods in Enzymology|January 1, 1994
Glutamyl endopeptidasesJ J Birktoft, K Breddam
Pageof 6